Whey protein-derived peptide sensing by enteroendocrine cells compared with osteoblast-like cells: Role of peptide length and peptide composition, focussing on products of β-lactoglobulin hydrolysis

The short-term satiating effect of whey protein intake is higher than that obtained with other dietary proteins. The molecular basis underlying the secretagogue effect of whey proteins on the release of cholecystokinin, a gut hormone involved in appetite suppression, has not been deeply investigated. Using STC-1 enteroendocrine cells we analysed the effects of synthetic peptides and protein hydrolysates. The hypothesis that specific molecular features in terms of short amino acid sequences released after enzymatic digestion may exert a primary role in the cholecystokinin secretagogue activity of dietary proteins was not supported. However, the length of the peptide fragments derived from a protein during enzymatic digestion is relevant to this activity. Regarding the complexities of how food can interact with different cellular systems, our data suggest a novel biological activity of ALPMH, a known bioactive peptide product of β-lactoglobulin digestion, on cell growth and a related signalling pathway in osteoblast-like cells.